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Anoctamin-6 (Small-conductance calcium-activated nonselective cation channel) (SCAN channel) (Transmembrane protein 16F)

 ANO6_HUMAN              Reviewed;         910 AA.
Q4KMQ2; A6NNM6; B9EGG0; E7ENK4; E9PB30; E9PCT2; Q8N3Q2;
13-SEP-2005, integrated into UniProtKB/Swiss-Prot.
17-OCT-2006, sequence version 2.
20-JUN-2018, entry version 122.
RecName: Full=Anoctamin-6;
AltName: Full=Small-conductance calcium-activated nonselective cation channel;
Short=SCAN channel;
AltName: Full=Transmembrane protein 16F;
Name=ANO6; Synonyms=TMEM16F;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16541075; DOI=10.1038/nature04569;
Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y.,
Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C.,
Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M.,
Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L.,
Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B.,
Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D.,
Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z.,
Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z.,
Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H.,
Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H.,
Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V.,
Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J.,
Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A.,
Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M.,
Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E.,
Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K.,
Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D.,
Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M.,
Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R.,
Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J.,
Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C.,
Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M.,
Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M.,
Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P.,
Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L.,
Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E.,
Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C.,
Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F.,
Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M.,
Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S.,
Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J.,
Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A.,
Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M.,
Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I.,
Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A.,
Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D.,
Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I.,
Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T.,
Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S.,
Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D.,
Kucherlapati R., Weinstock G., Gibbs R.A.;
"The finished DNA sequence of human chromosome 12.";
Nature 440:346-351(2006).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
TISSUE=Placenta, and Testis;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 772-910 (ISOFORM 1/2).
TISSUE=Adipose tissue;
PubMed=17974005; DOI=10.1186/1471-2164-8-399;
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
"The full-ORF clone resource of the German cDNA consortium.";
BMC Genomics 8:399-399(2007).
[4]
TISSUE SPECIFICITY.
PubMed=15067359;
Katoh M., Katoh M.;
"Identification and characterization of TMEM16E and TMEM16F genes in
silico.";
Int. J. Oncol. 24:1345-1349(2004).
[5]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-493.
TISSUE=Liver;
PubMed=19159218; DOI=10.1021/pr8008012;
Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
"Glycoproteomics analysis of human liver tissue by combination of
multiple enzyme digestion and hydrazide chemistry.";
J. Proteome Res. 8:651-661(2009).
[6]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=20056604; DOI=10.1074/jbc.M109.065367;
Schreiber R., Uliyakina I., Kongsuphol P., Warth R., Mirza M.,
Martins J.R., Kunzelmann K.;
"Expression and function of epithelial anoctamins.";
J. Biol. Chem. 285:7838-7845(2010).
[7]
FUNCTION, SUBCELLULAR LOCATION, AND INVOLVEMENT IN SCOTT SYNDROME.
PubMed=21107324; DOI=10.1038/nature09583;
Suzuki J., Umeda M., Sims P.J., Nagata S.;
"Calcium-dependent phospholipid scrambling by TMEM16F.";
Nature 468:834-838(2010).
[8]
REVIEW.
PubMed=21642943; DOI=10.1038/aps.2011.48;
Duran C., Hartzell H.C.;
"Physiological roles and diseases of Tmem16/Anoctamin proteins: are
they all chloride channels?";
Acta Pharmacol. Sin. 32:685-692(2011).
[9]
REVIEW.
PubMed=21607626; DOI=10.1007/s00424-011-0975-9;
Kunzelmann K., Tian Y., Martins J.R., Faria D., Kongsuphol P.,
Ousingsawat J., Thevenod F., Roussa E., Rock J., Schreiber R.;
"Anoctamins.";
Pflugers Arch. 462:195-208(2011).
[10]
FUNCTION.
PubMed=22006324; DOI=10.1073/pnas.1108094108;
Martins J.R., Faria D., Kongsuphol P., Reisch B., Schreiber R.,
Kunzelmann K.;
"Anoctamin 6 is an essential component of the outwardly rectifying
chloride channel.";
Proc. Natl. Acad. Sci. U.S.A. 108:18168-18172(2011).
[11]
SUBCELLULAR LOCATION.
PubMed=22075693; DOI=10.1152/ajpcell.00140.2011;
Duran C., Qu Z., Osunkoya A.O., Cui Y., Hartzell H.C.;
"ANOs 3-7 in the anoctamin/Tmem16 Cl- channel family are intracellular
proteins.";
Am. J. Physiol. 302:C482-C493(2012).
[12]
REVIEW.
PubMed=22302790; DOI=10.1113/expphysiol.2011.058214;
Winpenny J.P., Gray M.A.;
"The anoctamin (TMEM16) gene family: calcium-activated chloride
channels come of age.";
Exp. Physiol. 97:175-176(2012).
[13]
REVIEW, AND ABSENCE OF CALCIUM-ACTIVATED CHLORIDE CHANNEL ACTIVITY.
PubMed=21984732; DOI=10.1113/expphysiol.2011.058198;
Scudieri P., Sondo E., Ferrera L., Galietta L.J.;
"The anoctamin family: TMEM16A and TMEM16B as calcium-activated
chloride channels.";
Exp. Physiol. 97:177-183(2012).
[14]
REVIEW, AND FUNCTION.
PubMed=21908539; DOI=10.1113/expphysiol.2011.058206;
Kunzelmann K., Schreiber R., Kmit A., Jantarajit W., Martins J.R.,
Faria D., Kongsuphol P., Ousingsawat J., Tian Y.;
"Expression and function of epithelial anoctamins.";
Exp. Physiol. 97:184-192(2012).
[15]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=22946059; DOI=10.1242/jcs.109553;
Tian Y., Schreiber R., Kunzelmann K.;
"Anoctamins are a family of Ca2+ activated Cl- channels.";
J. Cell Sci. 125:4991-4998(2012).
[16]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[17]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25944712; DOI=10.1002/pmic.201400617;
Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M.,
Ayoub D., Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
"N-terminome analysis of the human mitochondrial proteome.";
Proteomics 15:2519-2524(2015).
-!- FUNCTION: Small-conductance calcium-activated nonselective cation
(SCAN) channel which acts as a regulator of phospholipid
scrambling in platelets and osteoblasts. Phospholipid scrambling
results in surface exposure of phosphatidylserine which in
platelets is essential to trigger the clotting system whereas in
osteoblasts is essential for the deposition of hydroxyapatite
during bone mineralization. Has calcium-dependent phospholipid
scramblase activity; scrambles phosphatidylserine,
phosphatidylcholine and galactosylceramide (By similarity). Can
generate outwardly rectifying chloride channel currents in airway
epithelial cells and Jurkat T lymphocytes.
{ECO:0000250|UniProtKB:Q6P9J9, ECO:0000269|PubMed:20056604,
ECO:0000269|PubMed:21107324, ECO:0000269|PubMed:21908539,
ECO:0000269|PubMed:22006324, ECO:0000269|PubMed:22946059}.
-!- ENZYME REGULATION: Exhibits synergistic gating by Ca(2+) and
voltage. Inhibited by some non-specific cation channel blockers
such as: ruthenium red, 2-aminoethyl diphenylborinate (2APB),
gadolinium and cadmium ions (By similarity). {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:20056604,
ECO:0000269|PubMed:21107324, ECO:0000269|PubMed:22075693,
ECO:0000269|PubMed:22946059}; Multi-pass membrane protein
{ECO:0000269|PubMed:20056604, ECO:0000269|PubMed:21107324,
ECO:0000269|PubMed:22075693, ECO:0000269|PubMed:22946059}.
Note=Shows an intracellular localization according to
PubMed:22075693.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=4;
Name=1;
IsoId=Q4KMQ2-1; Sequence=Displayed;
Name=2;
IsoId=Q4KMQ2-2; Sequence=VSP_042893;
Note=No experimental confirmation available.;
Name=3;
IsoId=Q4KMQ2-3; Sequence=VSP_046819;
Note=Gene prediction based on EST data.;
Name=4;
IsoId=Q4KMQ2-4; Sequence=VSP_046820;
Note=Gene prediction based on EST data.;
-!- TISSUE SPECIFICITY: Expressed in embryonic stem cell, fetal liver,
retina, chronic myologenous leukemia and intestinal cancer.
{ECO:0000269|PubMed:15067359}.
-!- DISEASE: Scott syndrome (SCTS) [MIM:262890]: A mild bleeding
disorder due to impaired surface exposure of procoagulant
phosphatidylserine (PS) on platelets and other blood cells,
following activation with Ca(2+)-elevating agents.
{ECO:0000269|PubMed:21107324}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- MISCELLANEOUS: The term 'anoctamin' was coined because these
channels are anion selective and have eight (OCT) transmembrane
segments. There is some dissatisfaction in the field with the Ano
nomenclature because it is not certain that all the members of
this family are anion channels or have the 8-transmembrane
topology.
-!- SIMILARITY: Belongs to the anoctamin family. {ECO:0000305}.
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EMBL; AC009248; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC009778; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC063924; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC098410; AAH98410.1; -; mRNA.
EMBL; BC136445; AAI36446.1; -; mRNA.
EMBL; AL833405; CAD38638.1; -; mRNA.
CCDS; CCDS31782.1; -. [Q4KMQ2-1]
CCDS; CCDS44865.1; -. [Q4KMQ2-4]
CCDS; CCDS44866.1; -. [Q4KMQ2-3]
CCDS; CCDS55819.1; -. [Q4KMQ2-2]
RefSeq; NP_001020527.2; NM_001025356.2. [Q4KMQ2-1]
RefSeq; NP_001136150.1; NM_001142678.1. [Q4KMQ2-3]
RefSeq; NP_001136151.1; NM_001142679.1. [Q4KMQ2-4]
RefSeq; NP_001191732.1; NM_001204803.1. [Q4KMQ2-2]
UniGene; Hs.505339; -.
ProteinModelPortal; Q4KMQ2; -.
BioGrid; 128218; 33.
IntAct; Q4KMQ2; 7.
MINT; Q4KMQ2; -.
STRING; 9606.ENSP00000409126; -.
TCDB; 1.A.17.1.4; the calcium-dependent chloride channel (ca-clc) family.
iPTMnet; Q4KMQ2; -.
PhosphoSitePlus; Q4KMQ2; -.
SwissPalm; Q4KMQ2; -.
BioMuta; ANO6; -.
DMDM; 116242820; -.
EPD; Q4KMQ2; -.
MaxQB; Q4KMQ2; -.
PaxDb; Q4KMQ2; -.
PeptideAtlas; Q4KMQ2; -.
PRIDE; Q4KMQ2; -.
ProteomicsDB; 62203; -.
ProteomicsDB; 62204; -. [Q4KMQ2-2]
Ensembl; ENST00000320560; ENSP00000320087; ENSG00000177119. [Q4KMQ2-1]
Ensembl; ENST00000423947; ENSP00000409126; ENSG00000177119. [Q4KMQ2-2]
Ensembl; ENST00000425752; ENSP00000391417; ENSG00000177119. [Q4KMQ2-4]
Ensembl; ENST00000441606; ENSP00000413137; ENSG00000177119. [Q4KMQ2-3]
GeneID; 196527; -.
KEGG; hsa:196527; -.
UCSC; uc001roo.4; human. [Q4KMQ2-1]
CTD; 196527; -.
DisGeNET; 196527; -.
EuPathDB; HostDB:ENSG00000177119.15; -.
GeneCards; ANO6; -.
H-InvDB; HIX0010565; -.
HGNC; HGNC:25240; ANO6.
HPA; HPA038958; -.
MalaCards; ANO6; -.
MIM; 262890; phenotype.
MIM; 608663; gene.
neXtProt; NX_Q4KMQ2; -.
OpenTargets; ENSG00000177119; -.
Orphanet; 806; Scott syndrome.
PharmGKB; PA164715690; -.
eggNOG; KOG2514; Eukaryota.
eggNOG; ENOG410XS4S; LUCA.
GeneTree; ENSGT00760000119015; -.
HOGENOM; HOG000006509; -.
HOVERGEN; HBG069519; -.
InParanoid; Q4KMQ2; -.
KO; K19500; -.
OMA; KHNIYYW; -.
OrthoDB; EOG091G01JF; -.
PhylomeDB; Q4KMQ2; -.
TreeFam; TF314265; -.
Reactome; R-HSA-2672351; Stimuli-sensing channels.
Reactome; R-HSA-6798695; Neutrophil degranulation.
ChiTaRS; ANO6; human.
GenomeRNAi; 196527; -.
PRO; PR:Q4KMQ2; -.
Proteomes; UP000005640; Chromosome 12.
Bgee; ENSG00000177119; -.
CleanEx; HS_ANO6; -.
ExpressionAtlas; Q4KMQ2; baseline and differential.
Genevisible; Q4KMQ2; HS.
GO; GO:0009986; C:cell surface; HDA:UniProtKB.
GO; GO:0034707; C:chloride channel complex; IDA:UniProtKB.
GO; GO:0005829; C:cytosol; IDA:HPA.
GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
GO; GO:0005622; C:intracellular; IDA:UniProtKB.
GO; GO:0016020; C:membrane; HDA:UniProtKB.
GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
GO; GO:0035579; C:specific granule membrane; TAS:Reactome.
GO; GO:0070821; C:tertiary granule membrane; TAS:Reactome.
GO; GO:0005227; F:calcium activated cation channel activity; IDA:UniProtKB.
GO; GO:0005229; F:intracellular calcium activated chloride channel activity; IMP:UniProtKB.
GO; GO:0017128; F:phospholipid scramblase activity; IEA:Ensembl.
GO; GO:0042803; F:protein homodimerization activity; IEA:Ensembl.
GO; GO:0005247; F:voltage-gated chloride channel activity; IMP:UniProtKB.
GO; GO:0005244; F:voltage-gated ion channel activity; ISS:UniProtKB.
GO; GO:0002543; P:activation of blood coagulation via clotting cascade; IMP:UniProtKB.
GO; GO:0032060; P:bleb assembly; IMP:UniProtKB.
GO; GO:0007596; P:blood coagulation; ISS:UniProtKB.
GO; GO:0035630; P:bone mineralization involved in bone maturation; IEA:Ensembl.
GO; GO:0061591; P:calcium activated galactosylceramide scrambling; IEA:Ensembl.
GO; GO:0061590; P:calcium activated phosphatidylcholine scrambling; IEA:Ensembl.
GO; GO:0061589; P:calcium activated phosphatidylserine scrambling; IEA:Ensembl.
GO; GO:0070588; P:calcium ion transmembrane transport; IGI:UniProtKB.
GO; GO:0006812; P:cation transport; IDA:UniProtKB.
GO; GO:1902476; P:chloride transmembrane transport; IGI:UniProtKB.
GO; GO:0006821; P:chloride transport; IMP:UniProtKB.
GO; GO:0002407; P:dendritic cell chemotaxis; IEA:Ensembl.
GO; GO:0034220; P:ion transmembrane transport; TAS:Reactome.
GO; GO:0045794; P:negative regulation of cell volume; IMP:UniProtKB.
GO; GO:0043312; P:neutrophil degranulation; TAS:Reactome.
GO; GO:0097045; P:phosphatidylserine exposure on blood platelet; IMP:UniProtKB.
GO; GO:0017121; P:phospholipid scrambling; IMP:UniProtKB.
GO; GO:0046931; P:pore complex assembly; IMP:UniProtKB.
GO; GO:0043065; P:positive regulation of apoptotic process; ISS:UniProtKB.
GO; GO:0030501; P:positive regulation of bone mineralization; IMP:UniProtKB.
GO; GO:2000353; P:positive regulation of endothelial cell apoptotic process; IMP:UniProtKB.
GO; GO:0034767; P:positive regulation of ion transmembrane transport; IMP:UniProtKB.
GO; GO:0090026; P:positive regulation of monocyte chemotaxis; IMP:UniProtKB.
GO; GO:0060100; P:positive regulation of phagocytosis, engulfment; ISS:UniProtKB.
GO; GO:1902304; P:positive regulation of potassium ion export; ISS:BHF-UCL.
GO; GO:0035590; P:purinergic nucleotide receptor signaling pathway; IMP:UniProtKB.
GO; GO:0035725; P:sodium ion transmembrane transport; IGI:UniProtKB.
InterPro; IPR032394; Anoct_dimer.
InterPro; IPR007632; Anoctamin.
InterPro; IPR031295; Anoctamin-6.
PANTHER; PTHR12308; PTHR12308; 1.
PANTHER; PTHR12308:SF21; PTHR12308:SF21; 1.
Pfam; PF16178; Anoct_dimer; 1.
Pfam; PF04547; Anoctamin; 1.
1: Evidence at protein level;
Alternative splicing; Cell membrane; Chloride; Chloride channel;
Complete proteome; Glycoprotein; Ion channel; Ion transport;
Lipid transport; Membrane; Polymorphism; Reference proteome;
Transmembrane; Transmembrane helix; Transport; Voltage-gated channel.
CHAIN 1 910 Anoctamin-6.
/FTId=PRO_0000191757.
TOPO_DOM 1 294 Cytoplasmic. {ECO:0000255}.
TRANSMEM 295 315 Helical. {ECO:0000255}.
TOPO_DOM 316 375 Extracellular. {ECO:0000255}.
TRANSMEM 376 396 Helical. {ECO:0000255}.
TOPO_DOM 397 454 Cytoplasmic. {ECO:0000255}.
TRANSMEM 455 475 Helical. {ECO:0000255}.
TOPO_DOM 476 513 Extracellular. {ECO:0000255}.
TRANSMEM 514 534 Helical. {ECO:0000255}.
TOPO_DOM 535 551 Cytoplasmic. {ECO:0000255}.
TRANSMEM 552 572 Helical. {ECO:0000255}.
TOPO_DOM 573 669 Extracellular. {ECO:0000255}.
TRANSMEM 670 690 Helical. {ECO:0000255}.
TOPO_DOM 691 725 Cytoplasmic. {ECO:0000255}.
TRANSMEM 726 746 Helical. {ECO:0000255}.
TOPO_DOM 747 824 Extracellular. {ECO:0000255}.
TRANSMEM 825 845 Helical. {ECO:0000255}.
TOPO_DOM 846 910 Cytoplasmic. {ECO:0000255}.
CARBOHYD 329 329 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 361 361 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 493 493 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:19159218}.
CARBOHYD 777 777 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 790 790 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 802 802 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
VAR_SEQ 1 23 MKKMSRNVLLQMEEEEDDDDGDI -> MFCAA (in
isoform 3). {ECO:0000305}.
/FTId=VSP_046819.
VAR_SEQ 23 23 I -> IGDVPASRRPFLTPHTHLPSSL (in isoform
2). {ECO:0000303|PubMed:15489334}.
/FTId=VSP_042893.
VAR_SEQ 843 910 HVIYSVKFFISYAIPDVSKRTKSKIQREKYLTQKLLHENHL
KDMTKNMGVIAERMIEAVDNNLRPKSE -> YLALLPRLGH
SGMILAHCNLRLPVDCCMCYRFVDEIRLLEQLTSDFIDSLY
YIFSISIISIFFSVTFFFLLLSLGPTPCFSVSNFLS (in
isoform 4). {ECO:0000305}.
/FTId=VSP_046820.
VARIANT 128 128 A -> T (in dbSNP:rs2162321).
/FTId=VAR_028109.
CONFLICT 837 837 F -> L (in Ref. 2; AAH98410).
{ECO:0000305}.
SEQUENCE 910 AA; 106165 MW; 8F7F1CB78FAAEB78 CRC64;
MKKMSRNVLL QMEEEEDDDD GDIVLENLGQ TIVPDLGSLE SQHDFRTPEF EEFNGKPDSL
FFNDGQRRID FVLVYEDESR KETNKKGTNE KQRRKRQAYE SNLICHGLQL EATRSVLDDK
LVFVKVHAPW EVLCTYAEIM HIKLPLKPND LKNRSSAFGT LNWFTKVLSV DESIIKPEQE
FFTAPFEKNR MNDFYIVDRD AFFNPATRSR IVYFILSRVK YQVINNVSKF GINRLVNSGI
YKAAFPLHDC KFRRQSEDPS CPNERYLLYR EWAHPRSIYK KQPLDLIRKY YGEKIGIYFA
WLGYYTQMLL LAAVVGVACF LYGYLNQDNC TWSKEVCHPD IGGKIIMCPQ CDRLCPFWKL
NITCESSKKL CIFDSFGTLV FAVFMGVWVT LFLEFWKRRQ AELEYEWDTV ELQQEEQARP
EYEARCTHVV INEITQEEER IPFTAWGKCI RITLCASAVF FWILLIIASV IGIIVYRLSV
FIVFSAKLPK NINGTDPIQK YLTPQTATSI TASIISFIII MILNTIYEKV AIMITNFELP
RTQTDYENSL TMKMFLFQFV NYYSSCFYIA FFKGKFVGYP GDPVYWLGKY RNEECDPGGC
LLELTTQLTI IMGGKAIWNN IQEVLLPWIM NLIGRFHRVS GSEKITPRWE QDYHLQPMGK
LGLFYEYLEM IIQFGFVTLF VASFPLAPLL ALVNNILEIR VDAWKLTTQF RRLVPEKAQD
IGAWQPIMQG IAILAVVTNA MIIAFTSDMI PRLVYYWSFS VPPYGDHTSY TMEGYINNTL
SIFKVADFKN KSKGNPYSDL GNHTTCRYRD FRYPPGHPQE YKHNIYYWHV IAAKLAFIIV
MEHVIYSVKF FISYAIPDVS KRTKSKIQRE KYLTQKLLHE NHLKDMTKNM GVIAERMIEA
VDNNLRPKSE


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